Recombinant Influenza A virus Hemagglutinin(HA)

Microbiology

HA

QDLPGNDNSTATLCLGHHAVPNGTLVKTITNDQIE VTNATELVQSSSTGKICNNPHRILDGINCTLIDAL LGDPHCDVFQDETWDLFVERSKAFSNCYPYDVPDY ASLRSLVASSGTLEFITEGFTWTGVTQNGGSNACK RGPDSGFFSRLNWLTKSGSTYPVLNVTMPNNDNFD KLYIWGVHHPSTNQEQTSLYVQASGRVTVSTRRSQ QTIIPNIGSRPWVRGLSSRISIYWTIVKPGDVLVI NSNGNLIAPRGYFKMRTGKSSIMRSDAPIDTCISE CITPNGSIPNDKPFQNVNKITYGACPKYVKQNTLK LATGMRNVPEKQT

Full Length

N-terminal 6xHis-tagged

Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. This attachment induces virion internalization of about two third of the virus particles through clathrin-dependent endocytosis and about one third through a clathrin- and caveolin-independent pathway. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induces an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore.

Greater than 85% as determined by SDS-PAGE.

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20C/-80C. The shelf life of lyophilized form is 12 months at -20C/-80C.

Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. This attachment induces virion internalization of about two third of the virus particles through clathrin-dependent endocytosis and about one third through a clathrin- and caveolin-independent pathway. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induces an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore.

Influenza viruses hemagglutinin family